H-Arg-Arg-Pro-Tyr-Ile-Leu-Ala-OH | 1024612-38-1

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: H-Arg-Arg-Pro-Tyr-Ile-Leu-Ala-OH
• 英文别名: (2S)-2-[[(2S)-2-[[(2S,3S)-2-[[(2S)-2-[[(2S)-1-[(2S)-2-[[(2S)-2-amino-5-(diaminomethylideneamino)pentanoyl]amino]-5-(diaminomethylideneamino)pentanoyl]pyrrolidine-2-carbonyl]amino]-3-(4-hydroxyphenyl)propanoyl]amino]-3-methylpentanoyl]amino]-4-methylpentanoyl]amino]propanoic acid
• CAS: 1024612-38-1
• 化学式: C₄₁H₆₉N₁₃O₉
• 分子量: 888.081
• InChiKey: NJSWDUQGRYCALZ-YLUGYNJDSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -2.7
• 重原子数：
  63
• 可旋转键数：
  26
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.63
• 拓扑面积：
  378
• 氢给体数：
  12
• 氢受体数：
  12

反应信息

• 作为产物：
  描述：

  Fmoc-L-脯氨酸 、 Fmoc-L-异亮氨酸 、 Fmoc-O-叔丁基-L-酪氨酸 、 Fmoc-Pbf-L-精氨酸 、 alkaline earth salt of/the/ methylsulfuric acid 、 alkaline earth salt of/the/ methylsulfuric acid 生成 H-Arg-Arg-Pro-Tyr-Ile-Leu-Ala-OH
  参考文献：
  名称：

  Peptide backbone modifications on the C-terminal hexapeptide of neurotensin

  摘要：

  To compare backbone-induced susceptibilities with affinity changes that are caused by side-chain modifications in the respective positions, structure activity relationship studies on a series of NT(8-13) analogues were performed providing valuable insights into the major requirement for neurotensin receptor recognition and activation. The data led us to highly potent NTR1 ligands and the generation of a pharmacophore model that will be helpful for the discovery of therapeutically relevant non-peptidic NTR1 agonists. (C) 2008 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2008.01.110

文献信息

• Structure-based exploration of an allosteric binding pocket in the NTS1 receptor using bitopic NT(8-13) derivatives and molecular dynamics simulations
  作者：Ralf Christian Kling、Carolin Burchardt、Jürgen Einsiedel、Harald Hübner、Peter Gmeiner

  DOI：10.1007/s00894-019-4064-x

  日期：2019.7

  Crystal structures of neurotensin receptor subtype 1 (NTS1) allowed us to visualize the binding mode of the endogenous peptide hormone neurotensin and its pharmacologically active C-terminal fragment NT(8-13) within the orthosteric binding pocket of NTS1. Beneath the orthosteric binding pocket, we detected a cavity that exhibits different sequences in the neurotensin receptor subtypes NTS1 and NTS2. In this

  神经降压素受体亚型1（NTS1）的晶体结构使我们能够可视化NTS1的正构结合口袋中内源性肽激素神经降压素及其药理活性C端片段NT（8-13）的结合模式。在正构结合袋下方，我们检测到一个在神经降压素受体亚型NTS1和NTS2中显示不同序列的腔。在这项研究中，我们使用NT（8-13）-Xaa类型的双向测试肽探索了这种变构结合口袋，其中NT（8-13）的C端部分连接至延伸至新发现口袋。我们的测试化合物对NTS1表现出纳摩尔亲和力，与亲本肽NT（8-13）相比，亚型选择性显着提高，并且在IP积累测定中具有激活受体的能力。
• Peptide backbone modifications on the C-terminal hexapeptide of neurotensin
  作者：Jürgen Einsiedel、Harald Hübner、Maud Hervet、Steffen Härterich、Susanne Koschatzky、Peter Gmeiner

  DOI：10.1016/j.bmcl.2008.01.110

  日期：2008.3

  To compare backbone-induced susceptibilities with affinity changes that are caused by side-chain modifications in the respective positions, structure activity relationship studies on a series of NT(8-13) analogues were performed providing valuable insights into the major requirement for neurotensin receptor recognition and activation. The data led us to highly potent NTR1 ligands and the generation of a pharmacophore model that will be helpful for the discovery of therapeutically relevant non-peptidic NTR1 agonists. (C) 2008 Elsevier Ltd. All rights reserved.